SERPINA1(Short peptide from AAT) Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
|Application ||WB, E|
|Calculated MW||H=47 KDa|
|Antigen Region||390-418 aa|
|Other Names||Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, Serpin A1, Short peptide from AAT, SPAAT, SERPINA1, AAT, PI|
|Target/Specificity||This SERPINA1(Short peptide from AAT) antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 390-418 amino acids from the C-terminal region of human SERPINA1(Short peptide from AAT).|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||SERPINA1(Short peptide from AAT) Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.|
|Cellular Location||Secreted. Endoplasmic reticulum. Note=The S and Z allele are not secreted effectively and accumulate intracellularly in the endoplasmic reticulum|
|Tissue Location||Ubiquitous. Expressed in leukocytes and plasma.|
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Provided below are standard protocols that you may find useful for product applications.
Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin.
Bollen A.,et al.DNA 2:255-264(1983).
Long G.L.,et al.Biochemistry 23:4828-4837(1984).
Rosenberg S.,et al.Nature 312:77-80(1984).
Ciliberto G.,et al.Cell 41:531-540(1985).
Nukiwa T.,et al.J. Biol. Chem. 261:15989-15994(1986).
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